[English] 日本語
Yorodumi
- PDB-5o0m: Deglycosylated Nogo Receptor with native disulfide structure 3 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5o0m
TitleDeglycosylated Nogo Receptor with native disulfide structure 3
ComponentsReticulon-4 receptor
KeywordsSIGNALING PROTEIN / nervous system / signaling / leucine-rich repeat domain / disulfide structure
Function / homology
Function and homology information


Roundabout binding / neuronal signal transduction / ganglioside GM1 binding / chondroitin sulfate binding / neuregulin receptor activity / ganglioside GT1b binding / negative regulation of axon regeneration / negative regulation of axon extension / corpus callosum development / negative chemotaxis ...Roundabout binding / neuronal signal transduction / ganglioside GM1 binding / chondroitin sulfate binding / neuregulin receptor activity / ganglioside GT1b binding / negative regulation of axon regeneration / negative regulation of axon extension / corpus callosum development / negative chemotaxis / positive regulation of Rho protein signal transduction / axonal growth cone / axonogenesis / positive regulation of GTPase activity / dendritic shaft / axon guidance / presynapse / negative regulation of neuron projection development / signaling receptor activity / heparin binding / growth cone / perikaryon / cell surface receptor signaling pathway / neuron projection / membrane raft / external side of plasma membrane / neuronal cell body / glutamatergic synapse / protein-containing complex binding / cell surface / endoplasmic reticulum / plasma membrane
Similarity search - Function
Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / Alpha-Beta Horseshoe / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Alpha Beta
Similarity search - Domain/homology
Reticulon-4 receptor
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsPronker, M.F. / Janssen, B.J.C.
Funding support Netherlands, 1items
OrganizationGrant numberCountry
NWOVidi 723.012.002 Netherlands
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2017
Title: Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self-interaction.
Authors: Pronker, M.F. / Tas, R.P. / Vlieg, H.C. / Janssen, B.J.C.
History
DepositionMay 16, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 18, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 8, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_id_CSD ..._citation.country / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 15, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Reticulon-4 receptor
B: Reticulon-4 receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,1287
Polymers72,0222
Non-polymers1,1065
Water7,584421
1
A: Reticulon-4 receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,6754
Polymers36,0111
Non-polymers6643
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Reticulon-4 receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4543
Polymers36,0111
Non-polymers4422
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)46.610, 112.070, 115.130
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Reticulon-4 receptor / Nogo receptor / NgR / Nogo-66 receptor / Nogo66 receptor-1 / NgR1


Mass: 36011.207 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Rtn4r, Ngr1, Nogor / Plasmid: pUPE107.03 / Cell (production host): HEK293 / Cell line (production host): HEK293 / Organ (production host): KIDNEY / Production host: Homo sapiens (human) / Variant (production host): GntI-/- / References: UniProt: Q99PI8
#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 421 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.09 Å3/Da / Density % sol: 41.08 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 0.05 M MIB buffer pH 5.0, 12.5% PEG1500

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 0.9999 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 22, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9999 Å / Relative weight: 1
ReflectionResolution: 1.9→56.03 Å / Num. obs: 48250 / % possible obs: 99.7 % / Redundancy: 4.6 % / CC1/2: 0.994 / Rsym value: 0.129 / Net I/σ(I): 6
Reflection shellResolution: 1.9→1.94 Å / Redundancy: 4.7 % / Mean I/σ(I) obs: 1.5 / CC1/2: 0.503 / Rsym value: 1.054 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1OZN
Resolution: 1.9→56.03 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 23.67
RfactorNum. reflection% reflection
Rfree0.2224 2428 5.05 %
Rwork0.1793 --
obs0.1815 48088 99.3 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.9→56.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4606 0 70 421 5097
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0034828
X-RAY DIFFRACTIONf_angle_d0.8696572
X-RAY DIFFRACTIONf_dihedral_angle_d12.2371752
X-RAY DIFFRACTIONf_chiral_restr0.032748
X-RAY DIFFRACTIONf_plane_restr0.003861
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.93880.33711460.30762659X-RAY DIFFRACTION99
1.9388-1.9810.32561420.27792594X-RAY DIFFRACTION99
1.981-2.0270.28781210.25992706X-RAY DIFFRACTION99
2.027-2.07770.26891450.22482607X-RAY DIFFRACTION99
2.0777-2.13390.27191430.22032693X-RAY DIFFRACTION99
2.1339-2.19670.23681400.20852627X-RAY DIFFRACTION99
2.1967-2.26760.24821490.20712666X-RAY DIFFRACTION100
2.2676-2.34870.23061300.19192694X-RAY DIFFRACTION100
2.3487-2.44270.23351430.19042655X-RAY DIFFRACTION99
2.4427-2.55390.21231530.18172637X-RAY DIFFRACTION99
2.5539-2.68850.22641230.16982695X-RAY DIFFRACTION99
2.6885-2.85690.21441440.17662676X-RAY DIFFRACTION99
2.8569-3.07750.23581500.18882689X-RAY DIFFRACTION99
3.0775-3.38720.25911380.17112722X-RAY DIFFRACTION99
3.3872-3.87720.15981530.14712730X-RAY DIFFRACTION99
3.8772-4.88450.17491370.12672752X-RAY DIFFRACTION99
4.8845-56.05940.2211710.16922858X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.22841.0684-1.20925.4813-0.26433.6350.15770.0764-0.5382-0.4986-0.2897-0.61120.74280.70580.05610.45940.19460.00130.34340.07840.2502-36.914560.737114.511
25.72470.79170.04175.0034-1.40094.27910.0986-0.1733-0.16630.0251-0.1796-0.10870.24950.3070.05260.21020.0369-0.04050.16710.01850.0933-45.616270.24819.1294
32.04712.5474-1.07346.1266-0.42847.28620.1237-0.1262-0.09530.488-0.08670.22950.2361-0.0554-0.00250.20710.066-0.01730.16760.0320.1807-52.598176.301920.7199
47.82931.3887-1.6978.32781.44138.10410.0471-0.28840.04820.27660.10440.15150.0798-0.1133-0.10610.15440.0702-0.0320.17010.06230.0517-55.560380.620417.5136
52.20650.78080.12764.82041.11776.35030.0076-0.12390.1390.3245-0.07880.1608-0.122-0.17870.02780.19940.0520.00150.13460.01810.1195-56.361885.98914.3252
67.74211.8215-0.03496.05321.36395.49640.0647-0.41360.49340.3165-0.18420.2747-0.3618-0.44680.05370.2450.0749-0.05530.1695-0.00660.1364-62.510292.358312.304
73.52723.379-0.20653.4745-0.6291.9086-0.19570.15150.6342-0.3609-0.09810.0236-0.6967-0.04660.22020.3030.0367-0.10760.23970.04260.2719-58.431797.65817.1925
84.06020.44040.12043.8784-1.87175.1443-0.1604-0.20120.4747-0.1746-0.07510.6913-0.328-0.34330.1930.23610.0407-0.09980.2234-0.04990.3288-72.575497.66471.643
93.02323.27640.49966.6809-2.34472.74340.5664-0.19651.25280.8743-0.18490.6082-0.571-0.6136-0.33740.65850.2274-0.04680.85-0.24621.0908-82.882101.922413.1409
101.9424-0.9128-0.59643.1810.64961.56790.0574-0.2328-0.19950.3170.0326-0.16760.26340.0555-0.07250.2032-0.0191-0.0860.19130.05860.1516-65.438411.994616.6122
112.4832-0.73691.2912.5792-0.71671.746-0.0156-0.14050.22210.1094-0.00390.1889-0.0959-0.11380.02250.1158-0.0220.05210.1381-0.01120.1233-86.20237.38579.0634
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 26 through 83 )
2X-RAY DIFFRACTION2chain 'B' and (resid 84 through 136 )
3X-RAY DIFFRACTION3chain 'B' and (resid 137 through 156 )
4X-RAY DIFFRACTION4chain 'B' and (resid 157 through 175 )
5X-RAY DIFFRACTION5chain 'B' and (resid 176 through 213 )
6X-RAY DIFFRACTION6chain 'B' and (resid 214 through 242 )
7X-RAY DIFFRACTION7chain 'B' and (resid 243 through 256 )
8X-RAY DIFFRACTION8chain 'B' and (resid 257 through 306 )
9X-RAY DIFFRACTION9chain 'B' and (resid 307 through 338 )
10X-RAY DIFFRACTION10chain 'A' and (resid 26 through 175 )
11X-RAY DIFFRACTION11chain 'A' and (resid 176 through 338 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more